Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors (Articolo in rivista) (literal)

Anno

• 2012-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1016/j.bmcl.2011.12.134 (literal)

Alternative label

• Truppo E, Supuran CT, Sandomenico A, Vullo D, Innocenti A, Di Fiore A, Alterio V, De Simone G, Monti SM. (2012)
  Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors
  in Bioorganic & medicinal chemistry letters (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Truppo E, Supuran CT, Sandomenico A, Vullo D, Innocenti A, Di Fiore A, Alterio V, De Simone G, Monti SM. (literal)

Pagina inizio

• 1560 (literal)

Pagina fine

• 1564 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 22 (literal)

Rivista

• Bioorganic & medicinal chemistry letters (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali

• 5 (literal)

Note

• ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Istituto di Biostrutture e Bioimmagini-CNR; Università degli Studi di Firenze, Polo Scientifico, Laboratorio di Chimica Bioinorganica. (literal)

Titolo

• Carbonic anhydrase VII is S-glutathionylated without loss of catalytic activity and affinity for sulfonamide inhibitors (literal)

Abstract

• Human carbonic anhydrase (CA, EC 4.2.1.1) VII is a cytosolic enzyme with high carbon dioxide hydration activity. Here we report an unexpected S-glutathionylation of hCA VII which has also been observed earlier in vivo for hCA III, another cytosolic isoform. Cys183 and Cys217 were found to be the residues involved in reaction with glutathione for hCA VII. The two reactive cysteines were then mutated and the corresponding variant (C183S/C217S) expressed. The native enzyme, the variant and the S-glutathionylated adduct (sgCA VII) as well as hCA III were fully characterized for their CO(2) hydration, esterase/phosphatase activities, and inhibition with sulfonamides. Our findings suggest that hCA VII could use the in vivo S-glutathionylation to function as an oxygen radical scavenger for protecting cells from oxidative damage, as the activity and affinity for inhibitors of the modified enzyme are similar to those of the wild type. (literal)

Prodotto di

• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• SIMONA MARIA MONTI (Unità di personale interno)
• VINCENZO ALTERIO (Persona)
• ANNA DI FIORE (Persona)
• GIUSEPPINA DE SIMONE (Unità di personale interno)
• ANNAMARIA SANDOMENICO (Unità di personale interno)

Incoming links:

Autore CNR di

• GIUSEPPINA DE SIMONE (Unità di personale interno)
• SIMONA MARIA MONTI (Unità di personale interno)
• VINCENZO ALTERIO (Persona)
• ANNA DI FIORE (Persona)
• ANNAMARIA SANDOMENICO (Unità di personale interno)

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Bioorganic & medicinal chemistry letters (Rivista)